Target intelligence / Profile preview

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 (B3GNT2)

Target
B3GNT2
Molecular classification
Enzyme, Glycosyltransferase, Type II transmembrane protein
01

Overview

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) is a type II transmembrane glycosyltransferase enzyme encoded by the B3GNT2 gene in humans. It catalyzes the transfer of N-acetylglucosamine (GlcNAc) from the donor UDP-GlcNAc to beta-galactoside acceptors, forming beta-1,3 glycosidic linkages and thereby participates in the biosynthesis of poly-N-acetyllactosamine chains. These structures are important in cell-cell and cell-matrix interactions, particularly in the biosynthesis of complex glycans in glycoproteins and glycolipids. Mutations in B3GNT2 are associated with glycosylation disorders, including muscular dystrophy-dystroglycanopathy and neurological syndromes such as lissencephaly. The enzyme’s catalytic mechanism involves coordinated substrate binding and inverting glycosyltransferase chemistry dependent on conserved active site residues and magnesium. Its activity and specificity make it a potential, but as yet largely unexploited, therapeutic target for modulating glycan structures in health and disease[1][3][5].

Other names
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2B3GNT2BETA3GNTB3GNT-2B3GN-T2B3GNT1Beta3Gn-T1Beta3Gn-T2B3GN-T1BGnT-2UDP-Galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7Beta-1,3-N-acetylglucosaminyltransferase BGnT-1Beta-1,3-N-acetylglucosaminyltransferase BGnT-2Beta-1,3-N-acetylglucosaminyltransferase 1
02

Mechanism of action

Glycosylation modulation via transfer of N-acetylglucosamine from UDP-GlcNAc to beta-galactoside, forming beta-1,3 glycosidic bonds [1][3][5]

03

Biological functions

Biosynthesis of poly-N-acetyllactosamine chainsGlycosphingolipids biosynthesisKeratan sulfate biosynthesis
04

Disease associations

Muscular dystrophy-dystroglycanopathyLissencephalyOther (see note below: The enzyme is broadly associated with glycosylation defects which may participate in multiple diseases)
05

Safety considerations

Potential for off-target glycosylation effects if therapeutically inhibited or manipulated (inferred from enzyme’s central role in complex glycan biosynthesis)

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